ID   SYL_PROMS               Reviewed;         856 AA.
AC   A2BR45;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=A9601_09721;
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=146891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP000551; ABM70256.1; -; Genomic_DNA.
DR   RefSeq; WP_011818411.1; NC_008816.1.
DR   AlphaFoldDB; A2BR45; -.
DR   SMR; A2BR45; -.
DR   STRING; 146891.A9601_09721; -.
DR   KEGG; pmb:A9601_09721; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..856
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009395"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   856 AA;  98448 MW;  757A16FBD1430C56 CRC64;
     MISPDKRYEA DTNLYNPSEI EKKWQSIWTE NNLYKTDELT ENSDKFYALS MFPYPSGNLH
     MGHVRNYVIT DLIARFQRFK GKSVLHPMGW DAFGLPAENA AIERGISPSV WTKKNISHMK
     SQLKLLGLSV DWDREFATCD ENYYIWTQYL FLELYKSGLV YQKESEVNWD PIDNTVLANE
     QVDSEGKSWR SGAVVEKKLL KQWFLRITNY ADELLKDLEK LDNWPERVKI MQDNWIGKSI
     GANINFNINT NPEKNITVFT TRPDTLFGVT YLAISVNHSL IKKITDQETI QDIENLKQYL
     KDNKNNELEK IGIKTSLIAI NPVNSEPIPI WVASYVLDEY GTGAVMGVPA HDLRDFEFAK
     KNNIDIKQVI VKDKSEQSNE LDNAYVENGY LINSNHYNGL ANTIAKLKIA EEGVNNGWAE
     NKIQYRLRDW LISRQRYWGC PIPIVNCKKC GAVPLNQSDL PVSLPKDIEI SANKINALGN
     NNDWINTTCP KCGIGARKET DTMDTFMCSS WYFLRYPSSK CSTKPFEKNE INKWLPVDQY
     VGGVEHAILH LLYARFFTKA LRDNELFDID EPFKKLLTQG MVQSAAYKNN KTGKYVSPSD
     ITDLSNPTDP IDNSKLEVLF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
     WGDTDVEGQF RFLSRIWKLY INCAKNINSK SNSHPDKEKS LIKSMNIAIK EISNDILNNQ
     FNTAISELMK FYNSLSNSIN DINNNLKIDA LKTFCILLAP FAPHIAEEIW HLIGFKKSVH
     LEHWPSFNAE ALKEDSYELV IQVNGKVRDK VNINNDMSED QIKELTLKRP NILKWTQDKE
     IRKIIIVKGK IMNIVV
//